Sequence-specific BamHI endonuclease. The proposed role of arginine residues in substrate binding and recognition.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference32 articles.
1. Recognition sequence of specific endonuclease BamHI from Bacillus amyloliquefaciens H
2. Purification and characterization of the sequence-specific endonuclease Bam HI.
3. Sequence-specific endonuclease Bam HI. Effect of hydrophobic reagents on sequence recognition and catalysis.
4. Sequence-specific endonuclease BamHI: relaxation of sequence recognition.
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1. Thermodynamic, Spectroscopic, and Equilibrium Binding Studies of DNA Sequence Context Effects in Four 40 Base Pair Deoxyoligonucleotides;Biochemistry;2000-06-09
2. Thermodynamic, Spectroscopic, and Equilibrium Binding Studies of DNA Sequence Context Effects in Six 22-Base Pair Deoxyoligonucleotides;Biochemistry;1999-08-01
3. Chemical modification of bovine pancreatic deoxyribonuclease with phenylglyoxal — The involvement of Arg-9 and Arg-41 in substrate binding;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1991-09
4. Exploring arylglyoxals as the arginine reactivity probes. A mechanistic investigation using the buffer and substituent effects;Bioorganic Chemistry;1991-09
5. [23] Protein chemical modification as probe of structure-function relationships;Protein \3- DNA Interactions;1991
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